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Literature summary for 2.7.11.1 extracted from
- Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity (2012), PLoS ONE, 7, e37371.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| X-ray crystal structure of toyocamycin bound to Rio1 at 2.0 A, toyocamycin binds in the ATP binding pocket of the protein | Archaeoglobus fulgidus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ATP | substrate inhibition. At ATP concentrations above 0.1 mM, kinase activity begins to drop until at 100 mM it becomes almost unmeasurable | Archaeoglobus fulgidus |  |
| Toyocamycin | toyocamycin binds in the ATP binding pocket of the protein more tightly than ATP/Mg2+ | Archaeoglobus fulgidus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0008 | - |
ATP | pH 8.0, 37°C | Archaeoglobus fulgidus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 30100 | - |
x * 30100, calculated from sequence, autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity | Archaeoglobus fulgidus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O28471 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + a protein | - |
Archaeoglobus fulgidus | ADP + a phosphoprotein | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| oligomer | x * 30100, calculated from sequence, autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity | Archaeoglobus fulgidus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| afRio1 kinase | - |
Archaeoglobus fulgidus |
| Rio1 kinase | - |
Archaeoglobus fulgidus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 76 | - |
Tm-value of unbound enzyme | Archaeoglobus fulgidus |
| 82 | - |
Tm-value in presence of ATP and Mg2+ | Archaeoglobus fulgidus |
| 82 | - |
Tm-value in presence of sangivamycin | Archaeoglobus fulgidus |
| 88 | - |
Tm-value in presence of toyocamycin | Archaeoglobus fulgidus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0071 | - |
ATP | pH 8.0, 37°C | Archaeoglobus fulgidus | |
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